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dc.contributor.authorBerghuis, Bojk A.
dc.contributor.authorRaducanu, Vlad-Stefan
dc.contributor.authorElshenawy, Mohamed
dc.contributor.authorJergic, Slobodan
dc.contributor.authorDepken, Martin
dc.contributor.authorDixon, Nicholas E.
dc.contributor.authorHamdan, Samir
dc.contributor.authorDekker, Nynke H.
dc.date.accessioned2017-11-09T06:33:07Z
dc.date.available2017-11-09T06:33:07Z
dc.date.issued2017-11-06
dc.identifier.citationBerghuis BA, Raducanu V-S, Elshenawy MM, Jergic S, Depken M, et al. (2017) What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments. Critical Reviews in Biochemistry and Molecular Biology: 1–15. Available: http://dx.doi.org/10.1080/10409238.2017.1394264.
dc.identifier.issn1040-9238
dc.identifier.issn1549-7798
dc.identifier.pmid29108427
dc.identifier.doi10.1080/10409238.2017.1394264
dc.identifier.urihttp://hdl.handle.net/10754/626136
dc.description.abstractSynchronizing the convergence of the two-oppositely moving DNA replication machineries at specific termination sites is a tightly coordinated process in bacteria. In Escherichia coli, a “replication fork trap” – found within a chromosomal region where forks are allowed to enter but not leave – is set by the protein–DNA roadblock Tus–Ter. The exact sequence of events by which Tus–Ter blocks replisomes approaching from one direction but not the other has been the subject of controversy for many decades. Specific protein–protein interactions between the nonpermissive face of Tus and the approaching helicase were challenged by biochemical and structural studies. These studies show that it is the helicase-induced strand separation that triggers the formation of new Tus–Ter interactions at the nonpermissive face – interactions that result in a highly stable “locked” complex. This controversy recently gained renewed attention as three single-molecule-based studies scrutinized this elusive Tus–Ter mechanism – leading to new findings and refinement of existing models, but also generating new questions. Here, we discuss and compare the findings of each of the single-molecule studies to find their common ground, pinpoint the crucial differences that remain, and push the understanding of this bipartite DNA–protein system further.
dc.description.sponsorshipFunding for this work has been provided by the Australian Research Council (DP150100956) (to NED), by King Abdullah University of Science and Technology through core funding to (S.M.H.) and a Competitive Research Award (CRG5) (to S.M.H. and NED); and by a VICI grant from the Netherlands Organization for Scientific Research and an ERC Consolidator Grant (DynGenome, no 312221) from the European Research Council (both to N.H.D.).
dc.publisherInforma UK Limited
dc.relation.urlhttp://www.tandfonline.com/doi/full/10.1080/10409238.2017.1394264
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectDNA–protein interactions
dc.subjectDNA replication
dc.subjectprokaryotic replication
dc.subjectreplication termination
dc.subjectreplisome
dc.subjectTus–Ter
dc.subjectsingle-molecule techniques
dc.subjectmagnetic tweezers
dc.titleWhat is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentChemical and Biological Engineering Program
dc.identifier.journalCritical Reviews in Biochemistry and Molecular Biology
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDepartment of Bionanoscience, Kavli institute of Nanoscience, Delft University of Technology, Delft, the Netherlands;
dc.contributor.institutionCentre for Medical and Molecular Bioscience, University of Wollongong, Wollongong, New South Wales, Australia
kaust.personRaducanu, Vlad-Stefan
kaust.personElshenawy, Mohamed
kaust.personHamdan, Samir
dc.relation.issupplementedbyDOI:10.6084/m9.figshare.5576410.v1
refterms.dateFOA2018-06-13T10:54:34Z
display.relations<b>Is Supplemented By:</b><br/> <ul><li><i>[Dataset]</i> <br/> Bojk A. Berghuis, Vlad-Stefan Raducanu, Elshenawy, M. M., Jergic, S., Depken, M., Dixon, N. E., Hamdan, S. M., &amp; Dekker, N. H. (2017). What is all this fuss about Tus? Comparison of recent findings from biophysical and biochemical experiments. <i>Taylor &amp; Francis</i>. https://doi.org/10.6084/M9.FIGSHARE.5576410.V1. DOI: <a href="https://doi.org/10.6084/m9.figshare.5576410.v1" >10.6084/m9.figshare.5576410.v1</a> Handle: <a href="http://hdl.handle.net/10754/663920" >10754/663920</a></a></li></ul>
dc.date.published-online2017-11-06
dc.date.published-print2018-01-02


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This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
Except where otherwise noted, this item's license is described as This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.